There are various forms of tropoelastin that typically appear to consist of two types of alternating domains: those rich in hydrophobic amino acids (responsible for the elastic properties) and those rich in lysin residues (responsible for cross-link formation). Hydrophobic and cross-linking domains are encoded in separate exons (Indik et al. 1987).
The gene for tropoelastin is believed to be present as a single copy in the mammalian genome, and is expressed in the form of multiple transcripts, distinguished by alternative splicing of the pre-mRNA (Indik et al, 1990; Oliver et al, 1987).
Previous recombinant work with tropoelastin has been reported by Indik et al (1990) who achieved modest expression of a natural human tropoelastin sequence from cDNA. Their product was unstable, the free polypeptide being rapidly degraded.
Bressan et al (1987) have reported the cloning of a defined naturally occurring segment of chick tropoelastin.